Very interesting, and simple English, article on alpha-synuclein in National Geographic:

We talk about Parkinson’s disease rather than Parkinson’s diseases, as if this disorder was a single thing. It is and it isn’t. Any two patients can differ greatly in when they first showed symptoms, what problems they experience, and how quickly their condition worsens. Some people only ever have difficulties with movement, while others suffer from full-blown dementia.

And yet, every case of Parkinson’s boils down to a protein called alpha-synuclein. Think of a protein as a sculpture made by folding up a long chain of beads. If alpha-synuclein folds correctly, it helps the neurons in our brain to send messages to one another. If it folds incorrectly, it becomes rowdy and sociable, gathering in large destructive clumps that wreck neurons.

http://phenomena.nationalgeographic....of-parkinsons/

Thanks for posting the link.

In my opinion, alpha-synuclein's key role in the etiology of PD is as good as proven, although the details remain:
- what causes the misfolding to start?
- when does an instance of misfolding become prion-like and "reproduce"?
- is a genetic predisposition to over express AS important?
- are rogue forms of AS communicable?

Clumping seems bad news, but in vitro tests [1] have shown that curcumin can reduce aggregation.

Tag johnt:alpha-synuclein

Reference:

[1] J Biol Chem. 2012 Mar 16;287(12):9193-9. doi: 10.1074/jbc.M111.325548. Epub 2012 Jan 20.
"Curcumin prevents aggregation in α-synuclein by increasing reconfiguration rate."
Ahmad B, Lapidus LJ.
http://www.ncbi.nlm.nih.gov/pubmed/22267729

John